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  Home > JCE Print > Journal of Chemical Education > Issues > 1998  > October  >
In the Laboratory
A 19F NMR Study of Enzyme Activity
Keith E. Peterman, Kevin Lentz, and Jeffery Duncan
York College of Pennsylvania, Physical Sciences Department, York, PA 17405
Cover
October 1998
Vol. 75 No. 10
p. 1283
Abstract
This basic enzyme activity laboratory experiment demonstrates how 19F NMR can be used in biochemical studies and presents the advantages of 19F NMR over 1H NMR for studies of this nature. N-Trifluoroacetylglycine was selected as a commercially available model fluorine-tagged substrate that readily undergoes acylase I-catalyzed hydrolysis to produce trifluoroacetic acid and glycine. Progress of the reaction was monitored by following conversion of the trifluoroacetyl moiety peak of N-trifluoroacetylglycine to trifluoroacetic acid. The extent of hydrolysis was determined by comparing integrated ratios of the two 19F NMR peaks. A plot of percent hydrolysis versus enzyme concentration was used to calculate unit activity of the enzyme. This is a viable laboratory experiment for junior/senior-level courses in instrumental analytical chemistry, biochemistry, molecular biology, or spectroscopy.
More Information
*  Citation
 Peterman, Keith E.; Lentz, Kevin; Duncan, Jeffery. J. Chem. Educ. 1998 75 1283.
*  Keywords
 biochem, instrumental methods, enzymes, NMR spectrometry, fluorine, laboratory instruction
*  History
 Created:
Last Updated:		 June 21, 1999
June 24, 2005
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